A bacteriophage tubulin homolog, PhuZ, forms a structure with the biochemical, structural, and functional properties of a simplified, bipolar spindle.

Neuronal networks balance flexibility with stability by allowing the firing rate of individual neurons within a network to vary over time, while ensuring that the average firing rate across the network remains constant.

Single-molecule imaging of CTCF and cohesin in live cells suggests that chromatin loops are dynamic structures that frequently form and fall apart.

A fast evolutionary approach to engineer membrane protein kinetic stability yields folded excitatory neurotransmitter transporters and provides insights into their denaturing pathway.

The tubulin GTPase cycle structurally modulates the microtubule cap, causing lattice expansion, which is an intermediate state involved in phosphate release and regulatory signaling.

A combination of cryo-electron microscopy of TPX2 bound to microtubules and in vitro reconstitution experiments reveals a novel microtubule interaction mode that explains how TPX2 promotes microtubule nucleation and stabilization.

GTPase-deficient microtubules are hyper-stable and have longer EB binding regions, demonstrating that EBs bind the GTP cap.

Crowding and metabolites in a simulated cellular environment alter protein conformations, modulate interactions of functionally related proteins, and lead to significant dynamic heterogeneity.

The EB binding region defines the length of the protective cap that stabilizes growing microtubules.